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A cooperative activation loop among SWI/SNF, γ-H2AX and H3 acetylation for DNA double-strand break repair
- A cooperative activation loop among SWI/SNF, γ-H2AX and H3 acetylation for DNA double-strand break repair
- Lee H.-S.; Park J.-H.; Kim S.-J.; Kwon S.-J.; Kwon J.
- Ewha Authors
- 권종범; 이한새
- SCOPUS Author ID
- Issue Date
- Journal Title
- EMBO Journal
- EMBO Journal vol. 29, no. 8, pp. 1434 - 1445
- SCI; SCIE; SCOPUS
- Document Type
- Although recent studies highlight the importance of histone modifications and ATP-dependent chromatin remodelling in DNA double-strand break (DSB) repair, how these mechanisms cooperate has remained largely unexplored. Here, we show that the SWI/SNF chromatin remodelling complex, earlier known to facilitate the phosphorylation of histone H2AX at Ser-139 (S139ph) after DNA damage, binds to γ-H2AX (the phosphorylated form of H2AX)-containing nucleosomes in S139ph-dependent manner. Unexpectedly, BRG1, the catalytic subunit of SWI/SNF, binds to γ-H2AX nucleosomes by interacting with acetylated H3, not with S139ph itself, through its bromodomain. Blocking the BRG1 interaction with γ-H2AX nucleosomes either by deletion or overexpression of the BRG1 bromodomain leads to defect of S139ph and DSB repair. H3 acetylation is required for the binding of BRG1 to γ-H2AX nucleosomes. S139ph stimulates the H3 acetylation on γ-H2AX nucleosomes, and the histone acetyltransferase Gcn5 is responsible for this novel crosstalk. The H3 acetylation on γ-H2AX nucleosomes is induced by DNA damage. These results collectively suggest that SWI/SNF, γ-H2AX and H3 acetylation cooperatively act in a feedback activation loop to facilitate DSB repair. © 2010 European Molecular Biology Organization.
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